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Ghosh U, Weliky DP. Rapid . Biochemistry. 2021;60(35):2637-2651doi: 10.1021/acs.biochem.1c00316.
Ghosh, U., & Weliky, D. P. (2021). Rapid . Biochemistry, 60(35), 2637-2651. https://doi.org/10.1021/acs.biochem.1c00316
Ghosh, Ujjayini, and Weliky, David P. "Rapid ." Biochemistry vol. 60,35 (2021): 2637-2651. doi: https://doi.org/10.1021/acs.biochem.1c00316
Ghosh U, Weliky DP. Rapid . Biochemistry. 2021 Sep 07;60(35):2637-2651. doi: 10.1021/acs.biochem.1c00316. Epub 2021 Aug 26. PMID: 34436856; PMCID: PMC8577873.
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Biochemistry. 2021 Sep 07;60(35):2637-2651. doi: 10.1021/acs.biochem.1c00316. Epub 2021 Aug 26.

Rapid .

Biochemistry

Ujjayini Ghosh, David P Weliky

Affiliations

  1. Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States.

PMID: 34436856 PMCID: PMC8577873 DOI: 10.1021/acs.biochem.1c00316

Abstract

An early step in cellular infection by a membrane-enveloped virus like HIV or influenza is joining (fusion) of the viral and cell membranes. Fusion is catalyzed by a viral protein that typically includes an apolar "fusion peptide" (fp) segment that binds the target membrane prior to fusion. In this study, the effects of nonhomologous HIV and influenza fp's on lipid acyl chain motion are probed with

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